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5IFP

STRUCTURE OF BETA-GALACTOSIDASE FROM ASPERGILLUS NIGER

Summary for 5IFP
Entry DOI10.2210/pdb5ifp/pdb
Descriptorbeta-galactosidase A, alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (10 entities in total)
Functional Keywordstim barrel, gh35, glycoside hydrolase, kinetics, protein conformation, carbohydrate metabolism, b-galactosidase, aspergillus niger, fungal protein, substrate specificity, prebiotics, galactooligosaccharides, gos, native, wildtype, hydrolase
Biological sourceAspergillus niger CBS 513.88
Cellular locationSecreted : A2QAN3
Total number of polymer chains1
Total formula weight117145.24
Authors
Rico-Diaz, A.,Ramirez-Escudero, M.,Vizoso Vazquez, A.,Cerdan, M.E.,Becerra, M.,Sanz-Aparicio, J. (deposition date: 2016-02-26, release date: 2017-04-19, Last modification date: 2024-01-10)
Primary citationRico-Diaz, A.,Ramirez-Escudero, M.,Vizoso-Vazquez, A.,Cerdan, M.E.,Becerra, M.,Sanz-Aparicio, J.
Structural features of Aspergillus niger beta-galactosidase define its activity against glycoside linkages.
FEBS J., 284:1815-1829, 2017
Cited by
PubMed: 28391618
DOI: 10.1111/febs.14083
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.71 Å)
Structure validation

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